Structure of PDB 3blo Chain A

Receptor sequence
>3bloA (length=349) Species: 542 (Zymomonas mobilis) [Search protein sequence]
RPRFSFSIAAREGKARTGTIEMKRGVIRTPAFMPVGTAATVKALKPETVR
ATGADIILGNTYHLMLRPGAERIAKLGGLHSFMGWDRPILTDSGGFQVMQ
SEEGVTFMLSPERSIEIQHLLGSDIVMAFDEVTPYPATPSRAASSMERSM
RWAKRSRDAFDSRKEQAENAALFGIQQGSVFENLRQQSADALAEIGFDGY
AVGGLSGGEGQDEMFRVLDFSVPMLPDDKPHYLMGVGKPDDIVGAVERGI
DMFDCPTGQAFTWDGPINIRNARFSEDLKPLDSECHCAVCQKWSRAYIHH
LIRAGEILGAMLMTEHNIAFYQQLMQKIRDSISEGRFSQFAQDFRARYF
3D structure
PDB3blo Investigation of Specificity Determinants in Bacterial tRNA-Guanine Transglycosylase Reveals Queuine, the Substrate of Its Eucaryotic Counterpart, as Inhibitor
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D102 D280 C318 C320 C323 H349
Catalytic site (residue number reindexed from 1) D92 D254 C285 C287 C290 H316
Enzyme Commision number 2.4.2.29: tRNA-guanosine(34) preQ1 transglycosylase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN A C318 C320 C323 H349 C285 C287 C290 H316
BS02 QEI A F106 D156 G229 G230 L231 M260 F96 D130 G203 G204 L205 M234
Gene Ontology
Molecular Function
GO:0008479 tRNA-guanosine(34) queuine transglycosylase activity
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0002099 tRNA wobble guanine modification
GO:0006400 tRNA modification
GO:0008033 tRNA processing
GO:0008616 queuosine biosynthetic process
GO:0101030 tRNA-guanine transglycosylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3blo, PDBe:3blo, PDBj:3blo
PDBsum3blo
PubMed23704982
UniProtP28720|TGT_ZYMMO Queuine tRNA-ribosyltransferase (Gene Name=tgt)

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